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Nucleic Acids Research, 1988, Vol. 16, No. 15 7545-7562
© 1988

Articles

Sequence analysis and transcriptional regulation of the Escherichia coil grpE gene, encoding a heat shock protein

Barbara Lipinska, Joshua King, Debbie Ang* and Costa Georgopoulos

Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center Salt Lake City, UT 84132, USA

*To whom correspondence should be addressed

Received March 10, 1988. Revised June 23, 1988. Accepted June 23, 1988.

We have sequenced the Escherichia coli grpE gene and shown that it encodes a 197-amino acid residue protein of 21,668-Mr. The predicted N-terminal amino acid sequence, as well as the overall amino acid composition agree well with that of the purified protein. From Northern analysis, we have shown that transcription of the grpE gene is under heat shock regulation, i.e., there is a rapid and transient increase in the rate of synthesis of grpE mRNA upon a shift-up in temperature. Forty-six bases upstream of the structural gene is a sequence closely related to the consensus heat shock promoter identified by Cowing et al. [Proc. Natl. Acad. Sci. U.S.A. 82, 2679-2683]. We have shown by S1 mapping and RNA sequencing that this is indeed the promoter for the grpE mRNA. It appears that all discernable transcription initiates only from this promoter, even under non-heat shock conditions.


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